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At least 235 records · Page 13Linked to original sources
PubMed1982

Lysozyme (muramidase) and alpha 1-anti-chymotrypsin as immunohistochemical tumour markers.

Since lysozyme and alpha 1-anti-chymotrypsin are constituents of normal histiocytes, their value as tumor cell markers in histiocytes neoplasias has been investigated using the indirect immunoperoxidase method and commercially available specific antisera on formaldehyde-fixed, paraffin-embedded 5 micrometers sections after pretreatment with pronase. The distribution of both markers was determined in 35 cases of malignant fibrous histiocytoma (MFH) and in 13 cases of malignant histiocytosis (MH). In 12 cases of MH both markers were found whereas in MFH alpha 1-antichymotrypsin was demonstrated in 26 and lysozyme in 16 cases only. In general, the staining for alpha 1-anti-chymotrypsin was more intense than the staining for lysozyme. A negative reaction does not exclude the possibility of MH or MFH. The presence of both constituents in tumours, however, can be considered as indicative of histiocytogenic origin and both can be useful markers for distinguishing histiocytic neoplasias from other tumours.

Chymotrypsin↗
PubMed1982

Fungitoxicity of muramidase. Ultrastructural damage to Candida albicans.

The antifungal activity of hen egg-white lysozyme was investigated in vitro using a hypotonic medium designed to support an anabolic cellular state with minimal growth stimulation. The pathogenic yeast Candida albicans was found to be sensitive to microgram amounts of hen egg-white lysozyme. This susceptibility was evidenced by sluggish growth and a dose-dependent killing process. Transmitted and scanning electron microscopic observations on lysozyme-treated C. albicans yeast cells revealed the following ultrastructural modifications: (1) plasmolysis, vacuolar expansion and wrinkled surface configuration; (2) unremitting accumulation of wall-like material that bulged into the periplasmic space; (3) qualitative changes in the organization of the wall. Ongoing structural modifications within the wall were highlighted with the cationic heavy metal dye ruthenium red. A disruption in the permeability of the cytoplasmic membrane was evidenced by modification 1 and by differential staining characteristics in light microscopy. The superimposed osmotic imbalance was identified as the cause of cell death. It is proposed that lysozyme acts on C. albicans by two distinct complementary mechanisms: enzymatic hydrolysis of N-glycosidic bonds that link polysaccharides and structural proteins of the wall; injury to the cytoplasmic membrane as a result of a cationic protein kind of interaction.

Candida albicans↗
PubMed1978

Activity and distribution of bacteriolytic N-acetyl-muramidase during growth of Acanthamoeba castellanii in axenic culture.

Bacteriolytic endo N-acetylmuramidase of Acanthamoeba castellanii has been studied. In amoeba cells the enzyme, like exo N-acetylglucosaminidase and acid phosphatase, is attached to the lysosomes, as it is sedimentable when homogenates are prepared in medium containing sucrose. The sedimentability could be abolished by treatment with Triton X-100, thermal disintegration or by osmotic shock. The sedimentability and acid pH optima of the enzyme are highly characteristic of lysosomes. However, in young cultures over 50 per cent of enzyme activity was secreted by amoeba cells to the environment. The enzyme activity changed with the phase of growth cycle. The activity of enzyme expressed as units per mg of amoeba protein or per constant number of cells has been found to increase over 10 fold on aging of amoeba cultures. The increase in enzyme activity was stopped by actidione. The possible mechanisms of the regulation of the activity of lysosomal enzyme synthesis by amoebae are discussed.

Acetylglucosaminidase↗
PubMed1993

Muramidase-mediated damage to Candida yeast cells. Histochemical and immunochemical characterization of accumulating wall-like material.

Hen egg-white lysozyme is known to be fungicidal to blastoconidia of Candida albicans under defined in vitro conditions. This lethal action leads to changes in the layering of cell wall and to plasmolysis, caused by unremitting accumulation of wall-like material between the yeast cell wall and cytoplasmic membrane. Here, several methods were applied on ultrathin sections to define the nature of wall-like material: histochemical staining with periodic acid-thiocarbohydrazide-silver proteinate, periodic acid-alkaline bismuth, and phosphotungstic acid at low pH; the localization of the carbohydrate residues with lectin-gold complex; immunocytochemical staining with monospecific antibodies, factor 1 and 6, which recognized major cell wall antigens. The wall-like material was almost uniformly highlighted with periodic acid-thiocarbohydrazide-silver proteinate, factor 1 antibody, concanavalin A-gold and wheat germ agglutinin-ovomucoid-gold, indicating the presence of mannoproteins and chitin. The serotype A-specific epitope recognized by factor 6 antibody was not detected in the wall-like material, although it was demonstrated in the outer cell wall layers after 2 h of exposure to lysozyme.

Antibodies, Monoclonal↗